PER6_VITVI
ID PER6_VITVI Reviewed; 15 AA.
AC P85995;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 11-DEC-2019, entry version 20.
DE RecName: Full=Peroxidase 6 {ECO:0000250|UniProtKB:Q42578};
DE EC=1.11.1.7;
DE Flags: Fragment;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RA Belchi-Navarro S., Almagro L., Bru R., Pedreno M.A.;
RL Submitted (JUL-2008) to UniProtKB.
CC -!- FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants,
CC biosynthesis and degradation of lignin, suberization, auxin catabolism,
CC response to environmental stresses such as wounding, pathogen attack
CC and oxidative stress. These functions might be dependent on each
CC isozyme/isoform in each plant tissue. {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2
CC H2O; Xref=Rhea:RHEA:56136, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:139520, ChEBI:CHEBI:139521; EC=1.11.1.7;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000250|UniProtKB:Q42578, ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q42578,
CC ECO:0000255|PROSITE-ProRule:PRU00297};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P84516,
CC ECO:0000255|PROSITE-ProRule:PRU00297}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Classical plant (class
CC III) peroxidase subfamily. {ECO:0000255|PROSITE-ProRule:PRU00297}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Secreted.
FT CHAIN <1..>15
FT /note="Peroxidase 6"
FT /id="PRO_0000363740"
FT UNSURE 1
FT /note="M or F"
FT UNSURE 4
FT /note="I or L"
FT UNSURE 7
FT /note="L or I"
FT UNSURE 14
FT /note="I or L"
FT NON_TER 1
FT NON_TER 15
SQ SEQUENCE 15 AA; 1560 MW; 9E390D9D05F06C58 CRC64;
MGNISPLTGT NGEIR